FMO DATABASE

FMODB ID: 2JKKR

Calculation Name: 5HIZ-A-Xray372

Preferred Name:

Target Type:

Ligand Name:

ligand 3-letter code:

PDB ID: 5HIZ

Chain ID: A

ChEMBL ID:

UniProt ID: P0C6Y4

Base Structure: X-ray

Registration Date: 2023-06-21

Reference: C. Watanabe, N. Tani, K. Kamisaka, T. Honma et al., Interaction energy analysis of Apo structure dataset on FMODB, To be published.

DOI:

IFIE MAP

IFIE Diagram

Modeling method

Optimization	MOE:Amber10:EHT
Restraint	OptAll
Protonation	MOE:Protonate 3D
Complement	MOE:Structure Preparation
Water	No
Procedure	Auto-FMO protocol ver. 2.20220422

FMO calculation

FMO method	FMO2-MP2/6-31G(d)
Fragmentation	Auto
Number of fragment	99
LigandResidueName
LigandFragmentNumber	0
LigandCharge	CYM=-1
Software	ABINIT-MP - Open Ver. 1 Rev. 23Q2 / 20200603(SMP)

Total energy (hartree)

FMO2-HF: Electronic energy	-714568.874456
FMO2-HF: Nuclear repulsion	676404.56028
FMO2-HF: Total energy	-38164.314176
FMO2-MP2: Total energy	-38276.995974

3D Structure

Snapshot

Ligand structure

Ligand Interaction

Ligand binding energy

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
N/A	N/A	N/A	N/A	N/A	N/A

Interactive mode: IFIE and PIEDA for fragment #1(A:7:GLY)

Summations of interaction energy for fragment #1(A:7:GLY)

IFIE [kcal/mol]	PIEDA [kcal/mol]				Charge transfer value [e]
IFIE SUMIFIE SUM at MP2 level.	ESElectro static interaction energy.	EXExchange-repulsion energy.	CT+mixCharge transfer and mixing terms energy.	DI(MP2)Dispersion energy.	q(I=>J)Charge transfer value from I to J fragments.
0.788	2.221	0.007	-0.621	-0.816	0.001

Interaction energy analysis for fragmet #1(A:7:GLY)

Snapshot

IFIE Diagram

Base fragment(s) of PIEDA/IFIE

Single fragment	Multi fragments
	Fragment list

Charge [e] FCHARGE : 0 / q_Mulliken : 0.052 / q_NPA : 0.010

Distance from base fragment(s) [Å]

Dist

Interaction energy by IFIE and PIEDA
[kcal/mol]

| Total | > | ES | > | EX | >
| CT+mix | > | DI(MP2) | >

Fragment charge [e]

FCHARGE q_Mulliken
q_NPA q(I=>J)

Residue

Res # RES

Sort

Graph Options

X Axis Label
Y Axis Max Y Axis Min
Display ES EX CT+mix DI(MP2)

frag_NumFragment number.	ChainChain species.	Res #Residue number.	RES3-letter code of amino acid residue, ligand and solvent molecule.	FCHARGEFormal charge [e].	q_MullikenFragment charge evaluated by Mulliken charge [e].	q_NPAFragment charge evaluated by natural population analysis(NPA) charge [e].	DISTDistance from Ligand [Å].	TotalIFIE at MP2 level [kcal/mol].	ESElectro static interaction energy by PIEDA [kcal/mol].	EXExchange-repulsion energy by PIEDA [kcal/mol].	CT+mixCharge transfer and mixing terms energy by PIEDA [kcal/mol].	DI(MP2)Dispersion energy by PIEDA [kcal/mol].	q(I=>J)Charge transfer value from I to J fragmens [e].
3	A	9	LEU	0	-0.007	0.008	3.803	0.518	1.758	0.000	-0.571	-0.669	0.001
4	A	10	LYS	1	0.960	0.992	5.072	0.013	0.034	-0.001	-0.005	-0.014	0.000
5	A	11	GLN	0	0.018	-0.009	8.863	0.066	0.066	0.000	0.000	0.000	0.000
6	A	12	ARG	1	0.816	0.896	11.967	-0.033	-0.033	0.000	0.000	0.000	0.000
7	A	13	SER	0	0.007	0.004	15.469	-0.017	-0.017	0.000	0.000	0.000	0.000
8	A	14	ILE	0	-0.012	0.000	18.076	0.018	0.018	0.000	0.000	0.000	0.000
9	A	15	LYS	1	0.872	0.916	20.355	0.002	0.002	0.000	0.000	0.000	0.000
10	A	16	ALA	0	0.008	0.007	21.452	0.008	0.008	0.000	0.000	0.000	0.000
11	A	17	GLU	-1	-0.786	-0.886	23.386	0.020	0.020	0.000	0.000	0.000	0.000
12	A	18	GLY	0	0.049	0.000	25.538	-0.002	-0.002	0.000	0.000	0.000	0.000
13	A	19	ASP	-1	-0.975	-0.967	28.151	0.000	0.000	0.000	0.000	0.000	0.000
14	A	20	GLY	0	0.070	0.047	31.536	0.002	0.002	0.000	0.000	0.000	0.000
15	A	21	ILE	0	-0.077	-0.042	28.389	-0.003	-0.003	0.000	0.000	0.000	0.000
16	A	22	VAL	0	0.058	0.034	27.591	0.003	0.003	0.000	0.000	0.000	0.000
17	A	23	GLY	0	-0.022	-0.012	25.882	-0.005	-0.005	0.000	0.000	0.000	0.000
18	A	24	GLU	-1	-0.801	-0.870	22.886	-0.021	-0.021	0.000	0.000	0.000	0.000
19	A	25	GLY	0	0.030	0.012	20.151	-0.006	-0.006	0.000	0.000	0.000	0.000
20	A	26	LYS	1	0.877	0.933	15.343	0.135	0.135	0.000	0.000	0.000	0.000
21	A	27	ALA	0	0.025	0.026	14.243	-0.011	-0.011	0.000	0.000	0.000	0.000
22	A	28	LEU	0	-0.011	-0.009	9.212	-0.031	-0.031	0.000	0.000	0.000	0.000
23	A	29	TYR	0	-0.033	-0.026	9.263	0.035	0.035	0.000	0.000	0.000	0.000
24	A	30	ASN	0	0.003	-0.007	5.852	-0.120	-0.120	0.000	0.000	0.000	0.000
25	A	31	ASN	0	-0.035	-0.022	7.901	-0.131	-0.131	0.000	0.000	0.000	0.000
26	A	32	GLU	-1	-0.734	-0.814	7.458	1.516	1.516	0.000	0.000	0.000	0.000
27	A	33	GLY	0	-0.034	-0.009	10.712	-0.144	-0.144	0.000	0.000	0.000	0.000
28	A	34	GLY	0	0.031	0.004	11.835	0.095	0.095	0.000	0.000	0.000	0.000
29	A	35	ARG	1	0.981	0.998	14.277	-0.305	-0.305	0.000	0.000	0.000	0.000
30	A	36	THR	0	0.030	0.025	12.584	0.100	0.100	0.000	0.000	0.000	0.000
31	A	37	PHE	0	-0.005	-0.026	11.029	-0.036	-0.036	0.000	0.000	0.000	0.000
32	A	38	MET	0	-0.019	0.020	10.439	0.032	0.032	0.000	0.000	0.000	0.000
33	A	39	TYR	0	-0.046	-0.047	4.512	0.050	0.100	-0.001	-0.002	-0.046	0.000
34	A	40	ALA	0	0.007	-0.008	10.412	-0.021	-0.021	0.000	0.000	0.000	0.000
35	A	41	PHE	0	0.025	0.014	12.694	0.001	0.001	0.000	0.000	0.000	0.000
36	A	42	ILE	0	-0.001	0.015	13.573	-0.012	-0.012	0.000	0.000	0.000	0.000
37	A	43	SER	0	-0.002	-0.012	17.343	0.009	0.009	0.000	0.000	0.000	0.000
38	A	44	ASP	-1	-0.783	-0.881	21.111	-0.115	-0.115	0.000	0.000	0.000	0.000
39	A	45	LYS	1	0.892	0.941	24.176	0.040	0.040	0.000	0.000	0.000	0.000
40	A	46	PRO	0	0.011	0.028	24.395	-0.004	-0.004	0.000	0.000	0.000	0.000
41	A	47	ASP	-1	-0.884	-0.960	26.332	-0.031	-0.031	0.000	0.000	0.000	0.000
42	A	48	LEU	0	-0.048	-0.009	22.914	0.006	0.006	0.000	0.000	0.000	0.000
43	A	49	ARG	1	0.810	0.866	23.700	-0.012	-0.012	0.000	0.000	0.000	0.000
44	A	50	VAL	0	-0.005	0.005	22.459	0.007	0.007	0.000	0.000	0.000	0.000
45	A	51	VAL	0	0.011	0.007	18.575	-0.010	-0.010	0.000	0.000	0.000	0.000
46	A	52	LYS	1	0.862	0.930	21.415	-0.026	-0.026	0.000	0.000	0.000	0.000
47	A	53	TRP	0	-0.039	-0.035	13.835	-0.020	-0.020	0.000	0.000	0.000	0.000
48	A	54	GLU	-1	-0.872	-0.924	19.995	0.088	0.088	0.000	0.000	0.000	0.000
49	A	55	PHE	0	-0.037	-0.037	15.543	-0.002	-0.002	0.000	0.000	0.000	0.000
50	A	56	ASP	-1	-0.886	-0.950	17.006	0.254	0.254	0.000	0.000	0.000	0.000
51	A	57	GLY	0	0.060	0.027	20.441	-0.015	-0.015	0.000	0.000	0.000	0.000
52	A	58	GLY	0	-0.059	-0.018	21.938	0.014	0.014	0.000	0.000	0.000	0.000
53	A	59	CYM	-1	-0.840	-0.887	21.670	0.081	0.081	0.000	0.000	0.000	0.000
54	A	60	ASN	0	-0.097	-0.085	20.142	0.017	0.017	0.000	0.000	0.000	0.000
55	A	61	THR	0	0.042	0.013	21.654	-0.007	-0.007	0.000	0.000	0.000	0.000
56	A	62	ILE	0	-0.025	0.000	16.624	0.008	0.008	0.000	0.000	0.000	0.000
57	A	63	GLU	-1	-0.753	-0.860	19.817	0.018	0.018	0.000	0.000	0.000	0.000
58	A	64	LEU	0	-0.057	-0.021	17.997	0.005	0.005	0.000	0.000	0.000	0.000
59	A	65	GLU	-1	-0.800	-0.895	17.203	0.014	0.014	0.000	0.000	0.000	0.000
60	A	66	PRO	0	0.011	-0.010	20.116	-0.007	-0.007	0.000	0.000	0.000	0.000
61	A	67	PRO	0	-0.017	0.016	20.204	-0.007	-0.007	0.000	0.000	0.000	0.000
62	A	68	ARG	1	0.884	0.932	17.717	0.117	0.117	0.000	0.000	0.000	0.000
63	A	69	LYS	1	0.966	0.978	19.497	0.055	0.055	0.000	0.000	0.000	0.000
64	A	70	PHE	0	-0.033	-0.013	17.001	-0.004	-0.004	0.000	0.000	0.000	0.000
65	A	71	LEU	0	0.049	0.027	20.922	0.009	0.009	0.000	0.000	0.000	0.000
66	A	72	VAL	0	-0.014	-0.009	18.777	-0.022	-0.022	0.000	0.000	0.000	0.000
67	A	73	ASP	-1	-0.843	-0.933	21.420	-0.115	-0.115	0.000	0.000	0.000	0.000
68	A	74	SER	0	-0.021	-0.026	22.928	-0.015	-0.015	0.000	0.000	0.000	0.000
69	A	75	PRO	0	-0.016	-0.012	25.507	0.008	0.008	0.000	0.000	0.000	0.000
70	A	76	ASN	0	-0.069	-0.037	28.031	0.004	0.004	0.000	0.000	0.000	0.000
71	A	77	GLY	0	0.020	0.027	30.005	0.006	0.006	0.000	0.000	0.000	0.000
72	A	78	ALA	0	0.026	0.029	25.953	-0.004	-0.004	0.000	0.000	0.000	0.000
73	A	79	GLN	0	-0.004	0.009	24.691	0.010	0.010	0.000	0.000	0.000	0.000
74	A	80	ILE	0	-0.027	-0.014	23.997	-0.012	-0.012	0.000	0.000	0.000	0.000
75	A	81	LYS	1	0.805	0.894	20.047	0.133	0.133	0.000	0.000	0.000	0.000
76	A	82	TYR	0	-0.001	-0.010	20.839	0.002	0.002	0.000	0.000	0.000	0.000
77	A	83	LEU	0	0.002	0.005	13.154	-0.002	-0.002	0.000	0.000	0.000	0.000
78	A	84	TYR	0	0.002	-0.020	17.098	0.011	0.011	0.000	0.000	0.000	0.000
79	A	85	PHE	0	0.011	-0.005	11.497	-0.001	-0.001	0.000	0.000	0.000	0.000
80	A	86	VAL	0	0.031	0.015	13.039	0.004	0.004	0.000	0.000	0.000	0.000
81	A	87	ARG	1	0.850	0.904	15.525	-0.031	-0.031	0.000	0.000	0.000	0.000
82	A	88	ASN	0	-0.036	-0.015	16.958	0.008	0.008	0.000	0.000	0.000	0.000
83	A	89	LEU	0	-0.015	0.027	9.681	0.023	0.023	0.000	0.000	0.000	0.000
84	A	90	ASN	0	0.071	0.025	10.168	-0.015	-0.015	0.000	0.000	0.000	0.000
85	A	91	THR	0	0.060	0.011	11.208	0.005	0.005	0.000	0.000	0.000	0.000
86	A	92	LEU	0	0.019	0.027	6.928	-0.035	-0.035	0.000	0.000	0.000	0.000
87	A	93	ARG	1	0.870	0.910	5.911	-0.916	-0.916	0.000	0.000	0.000	0.000
88	A	94	ARG	1	0.795	0.884	7.436	-0.099	-0.099	0.000	0.000	0.000	0.000
89	A	95	GLY	0	0.033	0.016	9.049	-0.064	-0.064	0.000	0.000	0.000	0.000
90	A	96	ALA	0	-0.013	-0.011	3.660	-0.215	-0.093	0.009	-0.043	-0.087	0.000
91	A	97	VAL	0	-0.015	-0.006	5.460	-0.381	-0.381	0.000	0.000	0.000	0.000
92	A	98	LEU	0	-0.004	-0.009	7.999	-0.072	-0.072	0.000	0.000	0.000	0.000
93	A	99	GLY	0	0.017	0.015	7.528	0.019	0.019	0.000	0.000	0.000	0.000
94	A	100	TYR	0	0.020	0.014	6.256	0.073	0.073	0.000	0.000	0.000	0.000
95	A	101	ILE	0	-0.039	-0.027	7.959	0.109	0.109	0.000	0.000	0.000	0.000
96	A	102	GLY	0	0.009	0.009	11.528	0.038	0.038	0.000	0.000	0.000	0.000
97	A	103	ALA	0	0.002	0.005	9.519	0.034	0.034	0.000	0.000	0.000	0.000
98	A	104	THR	0	-0.105	-0.041	11.495	0.023	0.023	0.000	0.000	0.000	0.000
99	A	105	VAL	0	-0.020	-0.004	13.509	0.079	0.079	0.000	0.000	0.000	0.000

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Interactive mode: IFIE and PIEDA for fragment #1(A:7:GLY)